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The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance

The proper distribution of proteins between the cytosol and various membrane-bound compartments is crucial for the functionality of eukaryotic cells. This requires the cooperation between protein transport machineries that translocate diverse proteins from the cytosol into these compartments and tar...

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Autores principales: Kunze, Markus, Berger, Johannes
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4585086/
https://www.ncbi.nlm.nih.gov/pubmed/26441678
http://dx.doi.org/10.3389/fphys.2015.00259
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author Kunze, Markus
Berger, Johannes
author_facet Kunze, Markus
Berger, Johannes
author_sort Kunze, Markus
collection PubMed
description The proper distribution of proteins between the cytosol and various membrane-bound compartments is crucial for the functionality of eukaryotic cells. This requires the cooperation between protein transport machineries that translocate diverse proteins from the cytosol into these compartments and targeting signal(s) encoded within the primary sequence of these proteins that define their cellular destination. The mechanisms exerting protein translocation differ remarkably between the compartments, but the predominant targeting signals for mitochondria, chloroplasts and the ER share the N-terminal position, an α-helical structural element and the removal from the core protein by intraorganellar cleavage. Interestingly, similar properties have been described for the peroxisomal targeting signal type 2 mediating the import of a fraction of soluble peroxisomal proteins, whereas other peroxisomal matrix proteins encode the type 1 targeting signal residing at the extreme C-terminus. The structural similarity of N-terminal targeting signals poses a challenge to the specificity of protein transport, but allows the generation of ambiguous targeting signals that mediate dual targeting of proteins into different compartments. Dual targeting might represent an advantage for adaptation processes that involve a redistribution of proteins, because it circumvents the hierarchy of targeting signals. Thus, the co-existence of two equally functional import pathways into peroxisomes might reflect a balance between evolutionary constant and flexible transport routes.
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spelling pubmed-45850862015-10-05 The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance Kunze, Markus Berger, Johannes Front Physiol Physiology The proper distribution of proteins between the cytosol and various membrane-bound compartments is crucial for the functionality of eukaryotic cells. This requires the cooperation between protein transport machineries that translocate diverse proteins from the cytosol into these compartments and targeting signal(s) encoded within the primary sequence of these proteins that define their cellular destination. The mechanisms exerting protein translocation differ remarkably between the compartments, but the predominant targeting signals for mitochondria, chloroplasts and the ER share the N-terminal position, an α-helical structural element and the removal from the core protein by intraorganellar cleavage. Interestingly, similar properties have been described for the peroxisomal targeting signal type 2 mediating the import of a fraction of soluble peroxisomal proteins, whereas other peroxisomal matrix proteins encode the type 1 targeting signal residing at the extreme C-terminus. The structural similarity of N-terminal targeting signals poses a challenge to the specificity of protein transport, but allows the generation of ambiguous targeting signals that mediate dual targeting of proteins into different compartments. Dual targeting might represent an advantage for adaptation processes that involve a redistribution of proteins, because it circumvents the hierarchy of targeting signals. Thus, the co-existence of two equally functional import pathways into peroxisomes might reflect a balance between evolutionary constant and flexible transport routes. Frontiers Media S.A. 2015-09-24 /pmc/articles/PMC4585086/ /pubmed/26441678 http://dx.doi.org/10.3389/fphys.2015.00259 Text en Copyright © 2015 Kunze and Berger. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Kunze, Markus
Berger, Johannes
The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance
title The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance
title_full The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance
title_fullStr The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance
title_full_unstemmed The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance
title_short The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance
title_sort similarity between n-terminal targeting signals for protein import into different organelles and its evolutionary relevance
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4585086/
https://www.ncbi.nlm.nih.gov/pubmed/26441678
http://dx.doi.org/10.3389/fphys.2015.00259
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